globalchange  > 影响、适应和脆弱性
项目编号: 1438634
项目名称:
Probing Dynamics and Structure of the Nanoparticle Protein Corona to Understand Its Impacts on Environmental Health and Safety
作者: Stephan Link
承担单位: William Marsh Rice University
批准年: 2013
开始日期: 2014-09-01
结束日期: 2017-08-31
资助金额: USD300000
资助来源: US-NSF
项目类别: Standard Grant
国家: US
语种: 英语
特色学科分类: Engineering - Chemical, Bioengineering, Environmental, and Transport Systems
英文关键词: protein ; np ; nanoparticle ; different protein ; dynamics ; structure ; goal ; nanoparticle protein corona ; abundant protein ; protein folding/unfolding ; protein corona ; environmental health ; corona change ; single protein detection level ; different nanoparticle ; model protein ; other protein ; donor-acceptor labeled protein ; pi ; individual nanoparticle ; protein coating
英文摘要: PI: Link, Stephan
Proposal Number: 1438634
Institution: William Marsh Rice University
Title: Probing Dynamics and Structure of the Nanoparticle Protein Corona to Understand Its Impacts on Environmental Health and Safety

The properties of nanoparticles (NPs) in biological fluids differ from their behavior in water due to the association of different proteins to the NP surface, forming a "protein corona" around the NPs. These proteins bind strongly to the NPs and affect the NPs' interactions with their environment. The goal of this proposal is to quantify the dynamics of proteins binding to NPs and to determine how the proteins may change their structure upon binding. The project will investigate model proteins, as well as proteins in blood plasma. The inclusion of experiments with whole plasma is an attractive feature of this proposed work, as whole plasma reflects the complexity of real-world conditions. The results of this research will be important for the understanding of the fate of nanoparticles, particularly, the bio-accumulation of nanoparticles in the food chain. In addition, understanding the dynamics of protein coating of NPs can be useful for the development of approaches that intentionally coat NPs with proteins in order to prevent other proteins from binding as a strategy to ensure that the NPs do not cause adverse effects on the environment. The PI and Co-PI are both active in outreach to the K-12 community and mentoring of undergraduate and graduate students.

While it is believed that the corona changes over time, as initially the most abundant proteins bind, but are then replaced with proteins that have the largest affinity, very little is known about the time scales of this dynamic exchange among different proteins. The goal of this proposal is to quantify the time-scales of protein-binding to NPs and to determine binding-induced structural changes of the proteins. Correlation spectroscopy will be used to determine the equilibrium protein-NP binding constant and number of bound proteins. The approach will be extended to measure competitive binding among different proteins to the same or possibly different nanoparticles. For protein folding/unfolding on NPs, the PIs will use CD spectroscopy on individual nanoparticles (with the goal of achieving single protein detection levels) and smFRET (single molecule fluorescence resonance energy transfer) microscopy of donor-acceptor labeled proteins. The investigators have unique and complementary strong expertise in the proposed area of research.
资源类型: 项目
标识符: http://119.78.100.158/handle/2HF3EXSE/95879
Appears in Collections:影响、适应和脆弱性
气候减缓与适应

Files in This Item:

There are no files associated with this item.


Recommended Citation:
Stephan Link. Probing Dynamics and Structure of the Nanoparticle Protein Corona to Understand Its Impacts on Environmental Health and Safety. 2013-01-01.
Service
Recommend this item
Sava as my favorate item
Show this item's statistics
Export Endnote File
Google Scholar
Similar articles in Google Scholar
[Stephan Link]'s Articles
百度学术
Similar articles in Baidu Scholar
[Stephan Link]'s Articles
CSDL cross search
Similar articles in CSDL Cross Search
[Stephan Link]‘s Articles
Related Copyright Policies
Null
收藏/分享
所有评论 (0)
暂无评论
 

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.